Recombinant Human ANKDD1A cell lysate
Cat.No. : | ANKDD1A-76HCL |
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Species : | Human |
Size : | 100 ul |
Storage Buffer : | 1X Sample Buffer (50 mM Tris-HCl, 2% SDS, 10% glycerol, 300 mM 2-mercaptoethanol, 0.01% Bromophenol blue) |
Applications : | Western Blot; |
Tag : | Non |
Gene Name : | ANKDD1A ankyrin repeat and death domain containing 1A [ Homo sapiens ] |
Official Symbol : | ANKDD1A |
Gene ID : | 348094 |
mRNA Refseq : | NM_182703.3 |
Protein Refseq : | NP_874362.3 |
UniProt ID : | Q495B1 |
Chromosome Location : | 15q22.31 |
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For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.
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Customer Reviews (4)
Write a reviewIts ability to accurately detect proteins and visualize their structures offers a valuable toolkit for advancing scientific understanding and discoveries.
The outstanding performance of ANKDD1A protein in both ELISA and protein electron microscopy structure analysis positions it as a highly valuable asset in diverse research areas.
By incorporating ANKDD1A protein into electron microscopy studies, researchers have gained valuable insights into protein interactions and conformational changes, contributing to a deeper understanding of complex cellular processes.
Its stability and well-defined structure make it an excellent candidate for visualizing and studying the three-dimensional arrangement of proteins at a high resolution.
Q&As (16)
Ask a questionCurrently, there is limited research on the role of ANKDD1A protein in cancer. However, some studies have reported altered expression of ANKDD1A in certain tumor types, suggesting a potential involvement in cancer development or progression. Further investigations are warranted to comprehensively evaluate the significance of ANKDD1A in cancer biology.
There is currently no direct evidence linking ANKDD1A protein to specific signaling pathways. However, its presence of the death domain suggests its potential involvement in cell death signaling cascades. Further studies are required to elucidate its role in signaling pathways and identify its interacting partners or downstream effectors.
ANKDD1A protein appears to be conserved across different species. Homologs of ANKDD1A have been identified in mammals, including humans, as well as in other vertebrates such as birds, reptiles, and fish. This conservation suggests that ANKDD1A protein may have important biological functions across diverse organisms.
The tissue-specific expression pattern of ANKDD1A protein has not been extensively studied. Limited expression data suggests that it may be expressed in multiple tissues, including the brain, liver, and heart. Further studies, such as mRNA or protein expression profiling in various tissues, are needed to determine the extent and specificity of ANKDD1A expression.
The involvement of ANKDD1A in signaling pathways has not been well-documented. However, based on the presence of a death domain, it is possible that ANKDD1A may participate in death receptor-mediated signaling pathways, such as apoptosis or inflammation. In-depth investigations and functional studies are required to determine the specific signaling pathways in which ANKDD1A is involved and its contributions to cellular processes.
As of now, there aren't any published knockout or knockdown studies specifically targeting ANKDD1A protein. This might be due to its relatively new discovery and limited understanding of its function. However, future studies involving functional analysis through knockout or knockdown techniques could provide valuable insights into the protein's role in cellular processes.
Limited functional characterization of ANKDD1A protein has been conducted thus far. It has been suggested to play a role in cell death signaling based on the presence of a death domain. However, more in-depth studies, including gain-of-function and loss-of-function experiments, are necessary to elucidate the specific functions and molecular mechanisms of ANKDD1A in cellular processes.
Currently, there are no reported interacting partners of ANKDD1A protein. Given its ankyrin repeats, it is possible that ANKDD1A protein may interact with other proteins or participate in protein-protein interactions, but this requires further investigation.
The regulation of ANKDD1A protein expression has not been extensively studied. However, its expression might be regulated at both transcriptional and post-transcriptional levels. Transcription factors and signaling pathways may influence the levels of ANKDD1A mRNA, while post-transcriptional mechanisms, such as alternative splicing or microRNA regulation, may also play a role in modulating the expression of ANKDD1A protein.
Currently, there are no known disease associations specifically linked to ANKDD1A protein. However, due to its potential involvement in cell growth and survival pathways, altered expression or function of ANKDD1A could potentially contribute to disease processes. Additional research is needed to determine if ANKDD1A has any disease associations.
The expression pattern of ANKDD1A protein has not been extensively studied. Limited data available from transcriptomic databases suggest that ANKDD1A mRNA is expressed in multiple tissues, including the brain, testis, kidney, and spleen. However, these findings need to be confirmed at the protein level through immunohistochemistry or Western blot analysis in various tissues and cell types to determine the specific expression pattern of ANKDD1A.
The exact roles of ANKDD1A in disease are largely unknown due to limited research. However, ANKDD1A has been implicated in certain disease processes. For example, a study found an association between genetic variations in the ANKDD1A gene and increased risk of ischemic stroke. This suggests a potential involvement of ANKDD1A in the pathogenesis of stroke or related vascular disorders. Further investigations are necessary to elucidate the functional significance and potential disease associations of ANKDD1A.
ANKDD1A protein shows varying degrees of conservation across different species. While the protein sequence itself may not be highly conserved, the presence of conserved domains, such as the ankyrin repeats and death domain, suggests functional significance. Comparative genomic analyses can provide a better understanding of the evolutionary conservation of ANKDD1A and its potential functional implications.
Currently, there are no known protein-protein interactions reported for ANKDD1A. However, this does not necessarily mean that there are no interactions. Further experimental studies, such as yeast two-hybrid screening or co-immunoprecipitation assays, could help identify potential interacting partners of ANKDD1A and provide insight into its cellular functions.
As of now, there are no known ANKDD1A mutations specifically associated with human diseases. However, it is important to note that the understanding of ANKDD1A's role in diseases is still limited due to the lack of comprehensive studies. Future research focusing on genomic analyses and functional studies may uncover potential disease-associated variations or mutations in the ANKDD1A gene.
There have been no reported genetic variants or mutations specifically associated with ANKDD1A protein so far. It is possible that such associations have not been investigated extensively, and future studies including genomic analyses and functional studies may uncover rare variants or mutations in ANKDD1A that could potentially impact its function or disease susceptibility.
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